TCPQ_HUMAN
ID TCPQ_HUMAN Reviewed; 548 AA.
AC P50990; A6NN54; B4DEM7; B4DQH4; Q4VBP8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=T-complex protein 1 subunit theta;
DE Short=TCP-1-theta;
DE AltName: Full=CCT-theta;
DE AltName: Full=Chaperonin containing T-complex polypeptide 1 subunit 8;
DE AltName: Full=Renal carcinoma antigen NY-REN-15;
GN Name=CCT8; Synonyms=C21orf112, CCTQ, KIAA0002;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8590283; DOI=10.1093/dnares/2.4.187;
RA Yamazaki M., Ono A., Watanabe K., Sasaki K., Tashiro H., Nomura T.;
RT "Nucleotide sequence surrounding the locus marker D21S246 on human
RT chromosome 21.";
RL DNA Res. 2:187-189(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Taudien S., Dagand E., Delabar J., Nordsiek G., Drescher B., Weber J.,
RA Schattevoy R., Menzel U., Yaspo M.-L., Rosenthal A.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Chondrosarcoma, and Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-16; 55-74; 156-165; 172-181; 283-296; 408-421;
RP 441-450 AND 510-520, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-65 (ISOFORM 1/2).
RX PubMed=7890169; DOI=10.1016/0378-1119(94)00880-2;
RA Kubota H., Hynes G., Willison K.;
RT "The eighth Cct gene, Cctq, encoding the theta subunit of the cytosolic
RT chaperonin containing TCP-1.";
RL Gene 154:231-236(1995).
RN [9]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [10]
RP INTERACTION WITH PACRG.
RX PubMed=14532270; DOI=10.1074/jbc.m309655200;
RA Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.;
RT "A product of the human gene adjacent to parkin is a component of Lewy
RT bodies and suppresses Pael receptor-induced cell death.";
RL J. Biol. Chem. 278:51901-51910(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND TYR-30, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318; LYS-400 AND LYS-466, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE
RP CHAPERONIN-CONTAINING T-COMPLEX.
RX PubMed=20080638; DOI=10.1073/pnas.0910268107;
RA Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C.,
RA Sheffield V.C.;
RT "BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and
RT mediate BBSome assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; TYR-30; SER-162; SER-213;
RP SER-269; SER-317 AND SER-537, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP FUNCTION, AND IDENTIFICATION IN THE CHAPERONIN-CONTAINING T-COMPLEX.
RX PubMed=25467444; DOI=10.1016/j.cell.2014.10.059;
RA Freund A., Zhong F.L., Venteicher A.S., Meng Z., Veenstra T.D., Frydman J.,
RA Artandi S.E.;
RT "Proteostatic control of telomerase function through TRiC-mediated folding
RT of TCAB1.";
RL Cell 159:1389-1403(2014).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-534, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-459, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-534 AND LYS-539, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-224; LYS-254; LYS-260; LYS-534
RP AND LYS-539, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a
CC molecular chaperone complex that assists the folding of proteins upon
CC ATP hydrolysis (PubMed:25467444). The TRiC complex mediates the folding
CC of WRAP53/TCAB1, thereby regulating telomere maintenance
CC (PubMed:25467444). As part of the TRiC complex may play a role in the
CC assembly of BBSome, a complex involved in ciliogenesis regulating
CC transports vesicles to the cilia (PubMed:20080638). The TRiC complex
CC plays a role in the folding of actin and tubulin (Probable).
CC {ECO:0000269|PubMed:20080638, ECO:0000269|PubMed:25467444,
CC ECO:0000305}.
CC -!- SUBUNIT: Component of the chaperonin-containing T-complex (TRiC), a
CC heterooligomeric complex of about 850 to 900 kDa that forms two stacked
CC rings, 12 to 16 nm in diameter (PubMed:20080638, PubMed:25467444).
CC Interacts with PACRG (PubMed:14532270). Interacts with DNAAF4 (By
CC similarity). {ECO:0000250|UniProtKB:P42932,
CC ECO:0000269|PubMed:14532270, ECO:0000269|PubMed:20080638,
CC ECO:0000269|PubMed:25467444}.
CC -!- INTERACTION:
CC P50990; P46379-2: BAG6; NbExp=3; IntAct=EBI-356507, EBI-10988864;
CC P50990; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-356507, EBI-741210;
CC P50990; P40227: CCT6A; NbExp=4; IntAct=EBI-356507, EBI-356687;
CC P50990; Q6ZTQ4: CDHR3; NbExp=3; IntAct=EBI-356507, EBI-12143631;
CC P50990; P42858: HTT; NbExp=4; IntAct=EBI-356507, EBI-466029;
CC P50990; Q8N7X4: MAGEB6; NbExp=3; IntAct=EBI-356507, EBI-6447163;
CC P50990; Q9UMY4: SNX12; NbExp=3; IntAct=EBI-356507, EBI-1752602;
CC P50990; P17987: TCP1; NbExp=2; IntAct=EBI-356507, EBI-356553;
CC P50990; P68363-2: TUBA1B; NbExp=3; IntAct=EBI-356507, EBI-25895616;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20080638}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20080638}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P42932}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P50990-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50990-2; Sequence=VSP_054692;
CC Name=3;
CC IsoId=P50990-3; Sequence=VSP_054691;
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02792.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D13627; BAA02792.2; ALT_INIT; mRNA.
DR EMBL; D42052; BAA07652.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF129075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK293705; BAG57138.1; -; mRNA.
DR EMBL; AK298801; BAG60936.1; -; mRNA.
DR EMBL; AL163249; CAB90433.1; -; Genomic_DNA.
DR EMBL; BC072001; AAH72001.1; -; mRNA.
DR EMBL; BC095470; AAH95470.1; -; mRNA.
DR EMBL; Z37163; CAA85520.1; -; mRNA.
DR CCDS; CCDS33528.1; -. [P50990-1]
DR CCDS; CCDS68180.1; -. [P50990-3]
DR CCDS; CCDS68181.1; -. [P50990-2]
DR PIR; PC4021; PC4021.
DR RefSeq; NP_001269836.1; NM_001282907.1. [P50990-2]
DR RefSeq; NP_001269838.1; NM_001282909.1. [P50990-3]
DR RefSeq; NP_006576.2; NM_006585.3. [P50990-1]
DR PDB; 6NR8; EM; 7.80 A; H/P=14-527.
DR PDB; 6NR9; EM; 8.50 A; H/P=14-527.
DR PDB; 6NRA; EM; 7.70 A; H/P=14-527.
DR PDB; 6NRB; EM; 8.70 A; H/P=14-527.
DR PDB; 6NRC; EM; 8.30 A; H/P=14-527.
DR PDB; 6NRD; EM; 8.20 A; H/P=14-527.
DR PDB; 6QB8; EM; 3.97 A; Q/q=1-548.
DR PDB; 7LUM; EM; 4.50 A; B/J=1-548.
DR PDB; 7LUP; EM; 6.20 A; B/J=1-548.
DR PDB; 7NVL; EM; 2.50 A; Q/q=1-548.
DR PDB; 7NVM; EM; 3.10 A; Q/q=1-548.
DR PDB; 7NVN; EM; 3.00 A; Q/q=1-548.
DR PDB; 7NVO; EM; 3.50 A; Q/q=1-548.
DR PDBsum; 6NR8; -.
DR PDBsum; 6NR9; -.
DR PDBsum; 6NRA; -.
DR PDBsum; 6NRB; -.
DR PDBsum; 6NRC; -.
DR PDBsum; 6NRD; -.
DR PDBsum; 6QB8; -.
DR PDBsum; 7LUM; -.
DR PDBsum; 7LUP; -.
DR PDBsum; 7NVL; -.
DR PDBsum; 7NVM; -.
DR PDBsum; 7NVN; -.
DR PDBsum; 7NVO; -.
DR AlphaFoldDB; P50990; -.
DR SMR; P50990; -.
DR BioGRID; 115933; 454.
DR ComplexPortal; CPX-6030; Chaperonin-containing T-complex.
DR CORUM; P50990; -.
DR DIP; DIP-38124N; -.
DR IntAct; P50990; 207.
DR MINT; P50990; -.
DR STRING; 9606.ENSP00000286788; -.
DR ChEMBL; CHEMBL4295775; -.
DR GlyGen; P50990; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P50990; -.
DR MetOSite; P50990; -.
DR PhosphoSitePlus; P50990; -.
DR SwissPalm; P50990; -.
DR BioMuta; CCT8; -.
DR DMDM; 9988062; -.
DR OGP; P50990; -.
DR REPRODUCTION-2DPAGE; IPI00784090; -.
DR REPRODUCTION-2DPAGE; P50990; -.
DR CPTAC; CPTAC-331; -.
DR CPTAC; CPTAC-332; -.
DR EPD; P50990; -.
DR jPOST; P50990; -.
DR MassIVE; P50990; -.
DR MaxQB; P50990; -.
DR PaxDb; P50990; -.
DR PeptideAtlas; P50990; -.
DR PRIDE; P50990; -.
DR ProteomicsDB; 3972; -.
DR ProteomicsDB; 4872; -.
DR ProteomicsDB; 56272; -. [P50990-1]
DR TopDownProteomics; P50990-1; -. [P50990-1]
DR Antibodypedia; 6409; 299 antibodies from 32 providers.
DR DNASU; 10694; -.
DR Ensembl; ENST00000286788.9; ENSP00000286788.4; ENSG00000156261.13. [P50990-1]
DR Ensembl; ENST00000540844.5; ENSP00000442730.1; ENSG00000156261.13. [P50990-3]
DR Ensembl; ENST00000626972.2; ENSP00000486921.1; ENSG00000156261.13. [P50990-2]
DR GeneID; 10694; -.
DR KEGG; hsa:10694; -.
DR MANE-Select; ENST00000286788.9; ENSP00000286788.4; NM_006585.4; NP_006576.2.
DR UCSC; uc002ynb.5; human. [P50990-1]
DR CTD; 10694; -.
DR DisGeNET; 10694; -.
DR GeneCards; CCT8; -.
DR HGNC; HGNC:1623; CCT8.
DR HPA; ENSG00000156261; Low tissue specificity.
DR MIM; 617786; gene.
DR neXtProt; NX_P50990; -.
DR OpenTargets; ENSG00000156261; -.
DR PharmGKB; PA26186; -.
DR VEuPathDB; HostDB:ENSG00000156261; -.
DR eggNOG; KOG0362; Eukaryota.
DR GeneTree; ENSGT00550000074783; -.
DR InParanoid; P50990; -.
DR OMA; WGLKYAV; -.
DR OrthoDB; 617040at2759; -.
DR PhylomeDB; P50990; -.
DR TreeFam; TF105699; -.
DR BRENDA; 3.6.4.B10; 2681.
DR PathwayCommons; P50990; -.
DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC.
DR Reactome; R-HSA-390450; Folding of actin by CCT/TriC.
DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR SignaLink; P50990; -.
DR BioGRID-ORCS; 10694; 776 hits in 1047 CRISPR screens.
DR ChiTaRS; CCT8; human.
DR GeneWiki; CCT8; -.
DR GenomeRNAi; 10694; -.
DR Pharos; P50990; Tbio.
DR PRO; PR:P50990; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P50990; protein.
DR Bgee; ENSG00000156261; Expressed in oocyte and 215 other tissues.
DR ExpressionAtlas; P50990; baseline and differential.
DR Genevisible; P50990; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005832; C:chaperonin-containing T-complex; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0044183; F:protein folding chaperone; IDA:FlyBase.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:ComplexPortal.
DR GO; GO:0046931; P:pore complex assembly; IEA:Ensembl.
DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; IMP:BHF-UCL.
DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; HMP:BHF-UCL.
DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; HMP:BHF-UCL.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
DR GO; GO:0006457; P:protein folding; IDA:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IMP:BHF-UCL.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR CDD; cd03341; TCP1_theta; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR012721; Chap_CCT_theta.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02346; chap_CCT_theta; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Cell projection; Chaperone; Cilium; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Isopeptide bond; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7"
FT CHAIN 2..548
FT /note="T-complex protein 1 subunit theta"
FT /id="PRO_0000128373"
FT REGION 529..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 30
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 400
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 466
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 505
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 224
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 459
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 534
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 539
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..78
FT /note="MALHVPKAPGFAQMLKEGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGM
FT NKMVINHLEKLFVTNDAATILRELEV -> MDQMV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054691"
FT VAR_SEQ 1..20
FT /note="MALHVPKAPGFAQMLKEGAK -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054692"
FT VARIANT 4
FT /note="H -> Q (in dbSNP:rs16983693)"
FT /id="VAR_052270"
FT VARIANT 409
FT /note="V -> I (in dbSNP:rs8129954)"
FT /id="VAR_052271"
FT CONFLICT 50
FT /note="N -> K (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="A -> V (in Ref. 1; BAA02792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 59621 MW; 566A6622BC2D15E9 CRC64;
MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN GMNKMVINHL
EKLFVTNDAA TILRELEVQH PAAKMIVMAS HMQEQEVGDG TNFVLVFAGA LLELAEELLR
IGLSVSEVIE GYEIACRKAH EILPNLVCCS AKNLRDIDEV SSLLRTSIMS KQYGNEVFLA
KLIAQACVSI FPDSGHFNVD NIRVCKILGS GISSSSVLHG MVFKKETEGD VTSVKDAKIA
VYSCPFDGMI TETKGTVLIK TAEELMNFSK GEENLMDAQV KAIADTGANV VVTGGKVADM
ALHYANKYNI MLVRLNSKWD LRRLCKTVGA TALPRLTPPV LEEMGHCDSV YLSEVGDTQV
VVFKHEKEDG AISTIVLRGS TDNLMDDIER AVDDGVNTFK VLTRDKRLVP GGGATEIELA
KQITSYGETC PGLEQYAIKK FAEAFEAIPR ALAENSGVKA NEVISKLYAV HQEGNKNVGL
DIEAEVPAVK DMLEAGILDT YLGKYWAIKL ATNAAVTVLR VDQIIMAKPA GGPKPPSGKK
DWDDDQND
